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| | ==Allophycocyanin from Thermosynechococcus vulcanus== | | ==Allophycocyanin from Thermosynechococcus vulcanus== |
| - | <StructureSection load='3dbj' size='340' side='right' caption='[[3dbj]], [[Resolution|resolution]] 2.90Å' scene=''> | + | <StructureSection load='3dbj' size='340' side='right'caption='[[3dbj]], [[Resolution|resolution]] 2.90Å' scene=''> |
| | == Structural highlights == | | == Structural highlights == |
| - | <table><tr><td colspan='2'>[[3dbj]] is a 8 chain structure with sequence from [http://en.wikipedia.org/wiki/Thermosynechococcus_vulcanus Thermosynechococcus vulcanus]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=3DBJ OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=3DBJ FirstGlance]. <br> | + | <table><tr><td colspan='2'>[[3dbj]] is a 8 chain structure with sequence from [https://en.wikipedia.org/wiki/Thermostichus_vulcanus Thermostichus vulcanus]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=3DBJ OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=3DBJ FirstGlance]. <br> |
| - | </td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=CYC:PHYCOCYANOBILIN'>CYC</scene></td></tr> | + | </td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 2.9Å</td></tr> |
| - | <tr id='NonStdRes'><td class="sblockLbl"><b>[[Non-Standard_Residue|NonStd Res:]]</b></td><td class="sblockDat"><scene name='pdbligand=MEN:N-METHYL+ASPARAGINE'>MEN</scene></td></tr> | + | <tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=CYC:PHYCOCYANOBILIN'>CYC</scene>, <scene name='pdbligand=MEN:N-METHYL+ASPARAGINE'>MEN</scene></td></tr> |
| - | <tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=3dbj FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3dbj OCA], [http://pdbe.org/3dbj PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=3dbj RCSB], [http://www.ebi.ac.uk/pdbsum/3dbj PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=3dbj ProSAT]</span></td></tr> | + | <tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=3dbj FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3dbj OCA], [https://pdbe.org/3dbj PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=3dbj RCSB], [https://www.ebi.ac.uk/pdbsum/3dbj PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=3dbj ProSAT]</span></td></tr> |
| | </table> | | </table> |
| | + | == Function == |
| | + | [https://www.uniprot.org/uniprot/B3VNK2_THEVL B3VNK2_THEVL] |
| | == Evolutionary Conservation == | | == Evolutionary Conservation == |
| | [[Image:Consurf_key_small.gif|200px|right]] | | [[Image:Consurf_key_small.gif|200px|right]] |
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| | ==See Also== | | ==See Also== |
| - | *[[Allophycocyanin|Allophycocyanin]] | + | *[[Allophycocyanin 3D structures|Allophycocyanin 3D structures]] |
| | == References == | | == References == |
| | <references/> | | <references/> |
| | __TOC__ | | __TOC__ |
| | </StructureSection> | | </StructureSection> |
| - | [[Category: Thermosynechococcus vulcanus]] | + | [[Category: Large Structures]] |
| - | [[Category: Adir, N]] | + | [[Category: Thermostichus vulcanus]] |
| - | [[Category: David, L]] | + | [[Category: Adir N]] |
| - | [[Category: Klartag, M]] | + | [[Category: David L]] |
| - | [[Category: McGregor, A]] | + | [[Category: Klartag M]] |
| - | [[Category: Cyanobacteria]]
| + | [[Category: McGregor A]] |
| - | [[Category: Energy transfer]]
| + | |
| - | [[Category: Light harvesting]]
| + | |
| - | [[Category: Photosynthesis]]
| + | |
| - | [[Category: Phycobilisome]]
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| Structural highlights
Function
B3VNK2_THEVL
Evolutionary Conservation
Check, as determined by ConSurfDB. You may read the explanation of the method and the full data available from ConSurf.
Publication Abstract from PubMed
Allophycocyanin (APC) is the primary pigment-protein component of the cores of the phycobilisome antenna complex. In addition to an extremely high degree of amino acid sequence conservation, the overall structures of APC from both mesophilic and thermophilic species are almost identical at all levels of assembly, yet APC from thermophilic organisms should have structural attributes that prevent thermally induced denaturation. We determined the structure of APC from the thermophilic cyanobacterium Thermosynechococcus vulcanus to 2.9 A, reaffirming the conservation of structural similarity with APC from mesophiles. We provide spectroscopic evidence that T. vulcanus APC is indeed more stable at elevated temperatures in vitro, when compared with the APC from mesophilic species. APC thermal and chemical stability levels are further enhanced when monitored in the presence of high concentrations of buffered phosphate, which increases the strength of hydrophobic interactions, and may mimic the effect of cytosolic crowding. Absorption spectroscopy, size-exclusion HPLC, and native gel electrophoresis also show that the thermally or chemically induced changes in the APC absorption spectra that result in the loss of the prominent 652-nm band in trimeric APC are not a result of physical monomerization. We propose that the bathochromic shift that occurs in APC upon trimerization is due to the coupling of the hydrophobicity of the alpha84 phycocyanobilin cofactor environment created by a deep cleft formed by the beta subunit with highly charged flanking regions. This arrangement also provides the additional stability required by thermophiles at elevated temperatures. The chemical environment that induces the bathochromic shift in APC trimers is different from the source of shifts in the absorption of monomers of the terminal energy acceptors APC(B) and L(CM), as visualized by the building of molecular models.
Allophycocyanin trimer stability and functionality are primarily due to polar enhanced hydrophobicity of the phycocyanobilin binding pocket.,McGregor A, Klartag M, David L, Adir N J Mol Biol. 2008 Dec 12;384(2):406-21. Epub 2008 Sep 16. PMID:18823993[1]
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.
See Also
References
- ↑ McGregor A, Klartag M, David L, Adir N. Allophycocyanin trimer stability and functionality are primarily due to polar enhanced hydrophobicity of the phycocyanobilin binding pocket. J Mol Biol. 2008 Dec 12;384(2):406-21. Epub 2008 Sep 16. PMID:18823993 doi:10.1016/j.jmb.2008.09.018
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